Photosynthesis and

Respiration in
Cyanobacteria

Secondary article
Article Contents
. Introduction
. Photosynthetic Electron Flow
. Respiratory Electron Flow

Wim FJ Vermaas, Arizona State University, Tempe, Arizona, USA

. Components Involved in Both Photosynthesis and

Respiration

Cyanobacteria are among the very few groups that can perform oxygenic photosynthesis
and respiration simultaneously in the same compartment, and some cyanobacterial
species are able to fix nitrogen. This combination of metabolic pathways is unusual and this
metabolic flexibility may be responsible for the evolutionary hardiness of the cyanobacteria
and their ability to thrive under a wide range of conditions.

Introduction
Cyanobacteria (formerly known as blue-green algae) are
thought to be among the evolutionarily oldest organisms:
putative microfossils have been found that are 3.5 billion
years old and that are attributed to cyanobacteria (Schopf,
1993). A main reason for the evolutionary hardiness of
cyanobacteria is their successful combination of eective
metabolic pathways. They are among the very few groups
that can perform oxygenic photosynthesis and respiration
simultaneously in the same compartment, and many
cyanobacterial species are able to x nitrogen. Therefore,
they can survive and prosper under a wide range of
environmental conditions.
The combination of photosynthesis and respiration in a
single compartment is thought to be quite unique, and the
ramications of this combination are reviewed. Photosynthesis and respiration require electron transport pathways that to a large extent are catalysed by protein
complexes in membranes. Figure 1 illustrates the compartmentalization of the cyanobacterial cell. The thylakoid
membrane, the internal membrane system that separates
the cytoplasm from the lumen and that is present in
virtually all cyanobacteria, contains both photosynthetic
and respiratory electron transport chains. These electron
transport chains intersect, and in part utilize the same
components in the membrane. Note that oxygenic photosynthesis (conversion of CO2 and water to sugars using the
energy from light) essentially is the reverse of respiration
(conversion of sugars to CO2 and water releasing energy).
The cytoplasmic membrane, separating the cytoplasm
from the periplasm, contains a respiratory electron
transport chain but not photosynthetic complexes in most
cyanobacteria. Therefore, in most cyanobacteria, photosynthetic electron transport occurs solely in thylakoids,
whereas respiratory electron ow takes place in both the
thylakoid and cytoplasmic membrane systems. Overviews
regarding aspects of cyanobacterial biochemistry and

. Regulation of Photosynthesis and Respiration

. Parallels to the Situation in Chloroplasts
. Acknowledgements

molecular biology related to photosynthesis and respiration are provided in Gantt (1994) and Schmetterer (1994).
The presence and simultaneous activity of photosynthetic and respiratory electron transport chains in the same
membrane system is unusual. A schematic representation
of the respiratory and photosynthetic electron transport
chains in cyanobacterial thylakoid membranes is shown in
Figure 2. As indicated, cyanobacteria utilize several redoxactive components in thylakoids for both photosynthesis
and respiration, including the plastoquinone (PQ) pool,
the cytochrome b6f complex, and the soluble electron
carriers in the lumen (in most species primarily plastocyanin, but cytochrome c553 (also known as cytochrome c6)
also occurs). In any case, the common use of components

Thylakoid
membrane
Thylakoid
lumen

Periplasm
Cytoplasm

Cell wall
Cytoplasmic
membrane

Figure 1 Outline of membranes and compartments in a cyanobacterial

cell. The cytoplasmic membrane separates the cytoplasm from the
periplasm; this membrane system is involved in respiration but not in
photosynthesis, and is yellow due to the presence of carotenoids. Thylakoid
membranes catalyse both photosynthetic and respiratory electron
transport; they contain chlorophyll and therefore are green. Thylakoids are
vase-shaped, and occur in pairs (the view represented here corresponds to
a cross-sectional cut through the vase). One pair of membranes envelops
the next pair, much like a set of Russian dolls. The space between a pair of
thylakoid membranes is the thylakoid lumen, into which protons are
deposited upon photosynthetic and respiratory electron transport in
thylakoids. The resulting proton gradient across the thylakoids is used for
ATP synthesis. The space between two pairs of thylakoids is contiguous with
the cytoplasm of the cell.

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Photosynthesis and Respiration in Cyanobacteria

NADPH NADP
Succinate Fumarate
NADPH NADP

Cytoplasm
Fdox

H2O

SDH

NDH-1

PS II

PQ

Fdred

cyt
b6f

PS I

O2 + H+

Ox

impediment in view of the stunning longevity with which

cyanobacteria have been a major presence in life on earth.
A short overview of photosynthetic electron ow will be
provided, followed by a summary of progress in the study
of respiratory electron ow in cyanobacteria. In the last
section, components involved in both photosynthesis and
respiration in cyanobacteria will be covered.

Thylakoid
membrane

Photosynthetic Electron Flow

H2O

O2 + H+

PC

Lumen

Figure 2 Schematic representation of the intersecting photosynthetic

and respiratory electron transport pathways in thylakoid membranes of the
cyanobacterium Synechocystis sp. PCC 6803. Arrows indicate electron
transfer reactions, and thunderbolts designate light that sets into motion
the redox reactions in the two photosystems. The thickness of each arrow is
an approximate indication of the rate of the corresponding reaction.
Electron transfer complexes that are specifically involved in photosynthetic
electron transfer are PS II and PS I, whereas those specific for respiratory
electron flow include NDH-1, SDH, and the terminal oxidase. PQ, cyt b6f
and PC are shared by both pathways. The electron transfer arrows involving
SDH are drawn in both directions, as the difference in midpoint redox
potentials between the PQ/PQH2 and fumarate/succinate redox couples is
small and therefore electron flow can occur in both directions depending
on the relative concentrations of PQ, PQH2, succinate and fumarate.
Abbreviations: cyt b6f, the cytochrome b6f complex; Fdox and Fdred,
ferredoxin in oxidized and reduced forms, respectively; NADP(H),
nicotinamide adenine dinucleotide phosphate (reduced form); NDH-1,
type 1 NADPH dehydrogenase; Ox, terminal oxidase; PC, plastocyanin;
PQ, plastoquinone; PS I, photosystem I; PS II, photosystem II; SDH,
succinate dehydrogenase.

for essentially opposite metabolic processes that occur at

the same time does not appear to be a signicant

The photosynthetic electron transport chain in cyanobacteria is essentially identical to that in plants, even though
some of the polypeptides that are part of electrontransporting enzymes appear to be of dierent evolutionary origin in the two systems. Indeed, chloroplasts in plants
are thought to have originated from cyanobacterial
ancestors. The photosynthetic electron transport chain of
oxygenic organisms has been reviewed extensively (for
example, Ort and Yocum, 1996; Hippler et al., 1998;
Whitmarsh, 1998), so only a brief summary will be
provided here. As indicated in Figure 2, photosystem II
(PS II) uses light energy to split water and to reduce the PQ
pool. Table 1 summarizes the protein components involved
with PS II and with other complexes mentioned in Figure 2.
Electrons are transported from the PQ pool to the
cytochrome b6f complex and from there to a soluble
electron carrier on the luminal side of the thylakoid
membrane. In cyanobacteria this soluble carrier may be
plastocyanin or cytochrome c553, depending on the species
and on the availability of copper (plastocyanin is a coppercontaining enzyme). Either of these soluble one-electron
carriers can reduce the oxidized PS I reaction centre
chlorophyll, P700 1 . This oxidized form of the reaction

Table 1 Major complexes involved with photosynthetic and respiratory electron flow in thylakoid membranes in cyanobacteria

Complex

Gene
designation

Photosystem II

Major proteins

Cofactors

Function

psb

D1, D2, CP43, CP47,

PsbO

Light-induced water splitting

and PQ reduction

Succinate dehydrogenase

sdh

SdhA, SdhB, SdhC

Mn, Ca, Cl, Fe, PQ,

chlorophyll, cyt b559,
pheophytin
Flavin, FeS centres

Type-1 NADPH
dehydrogenase
Cytochrome b6 f

ndh

NdhA-L

FeS centres

pet

2 cyt b, cyt f (cyt c), FeS

Photosystem I

psa

Cytochrome oxidase

cta

cyt b6, cyt f, Rieske,

subunit IV
PsaA, PsaB and other
Psa proteins
CtaC, CtaD, CtaE

Chlorophyll, vitamin K1,

FeS centres
CuA, CuB, Mg, cyt a, cyt a3

Succinate oxidation and PQ

reduction
NADPH oxidation and PQ
reduction
PQH2 oxidation and PC/cyt
c553 reduction
Light-induced PC/cyt c553
oxidation and Fd reduction
Cyt c oxidation and O2
reduction

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Photosynthesis and Respiration in Cyanobacteria

centre chlorophyll is formed by a light-induced transfer of

an electron from PS I to ferredoxin (Fd) and eventually to
NADP. Reduced NADP can be used for CO2 xation.
Photosynthetic electron transfer leads to a proton
gradient across the thylakoid membrane. In PS II, protons
are released into the lumen upon water splitting, and
protons formed upon plastoquinol oxidation by the
cytochrome b6f complex are released into the lumen as
well. The proton gradient across the thylakoid membrane
is used for ATP synthesis by the ATP synthase in the
thylakoid; this ATP may be applied for CO2 xation and
for other cell processes.
One important dierence between cyanobacteria and
plants is that the stoichiometry of PS I and PS II in at least
some species of cyanobacteria is much larger than 1,
whereas in higher plants an equal amount of PS I and PS II
is the rule. For example, in the cyanobacterium Synechocystis sp. PCC 6803 the PS I/PS II ratio is about 5 (see Shen
et al., 1993). One possible explanation for this unusual
stoichiometry in cyanobacteria is the involvement of PS I
in a signicant amount of cyclic electron ow around this
photosystem, in which electrons would ow from PS I/Fd
back to PQ and cytochrome b6f, and from there to PS I
again (reviewed by Bendall and Manasse, 1995). This
electron transport pathway should contribute to a proton
gradient, which could be used for ATP synthesis, but
would not lead to net NADP reduction. However, a high
rate of cyclic electron ow around PS I in cyanobacteria
cannot be demonstrated experimentally. Another and
probably more plausible reason for the relatively large
amount of PS I in cyanobacteria is the abundance of
respiratory electron transfer pathways into the PQ pool,
whereas the capacity of respiratory electron ow out of the
PQ pool may be more limited (see the next section).
Therefore, an abundance of PS I may guarantee a rather
oxidized PQ pool in the light, which is important to
minimize photodamage (reviewed by Andersson and
Barber, 1996). Moreover, the high amount of PS I may
serve to compete eectively with cytochrome oxidase for
electrons when light is available, thus maximizing the
number of electrons that can be used for CO2 xation.

Respiratory Electron Flow

The respiratory pathways in cyanobacteria have long been
unclear or misunderstood. However, considerable insight
has now been obtained in this important aspect of
cyanobacterial physiology, primarily by making use of
mutants lacking specic proteins. Much of this work has
been performed on Synechocystis sp. PCC 6803, which is
very amenable to targeted genetic modication (Vermaas,
1996) and which was the rst cyanobacterium for which a
complete genomic sequence has become available (Kaneko
et al., 1996). It has now been realized that the main
respiratory electron transport activity into the PQ pool in

cyanobacterial thylakoids involves succinate dehydrogenase (SDH) activity rather than electron ow from
NAD(P)H (Cooley et al., 2000); NADPH appears to be
used preferentially for carbon xation processes. The
corollary of this new concept is that cyanobacteria are able
to generate succinate as a respiratory intermediate, and
therefore should have a (modied) citric acid cycle.
According to the older literature, a citric acid cycle was
presumed to be nonfunctional in cyanobacteria as a key
enzyme, 2-oxoglutarate dehydrogenase, was absent (reviewed in Stanier and Cohen-Bazire, 1977). Indeed, this is
true according to the genomic sequence of Synechocystis
sp. PCC 6803, but this organism is able to convert 2oxoglutarate to succinate in the absence of a traditional 2oxoglutarate dehydrogenase complex (Cooley et al., 2000),
making use of an alternate pathway.

NAD(P)H oxidation
The cyanobacterial equivalent of the mitochondrial and
bacterial type-1 NADPH dehydrogenase (NDH-1) is an
enzyme complex similar to the 14-subunit NDH-1 complex
from Escherichia coli, except that three subunits involved
with substrate binding are not apparent from the
cyanobacterial genome. Probably related to this observation, the preferred substrate of cyanobacterial NDH-1 is
NADPH rather than NADH. Upon inactivation of ndhB,
the gene for one of the essential NDH-1 subunits, mutants
required high CO2 for growth (Ogawa, 1991) and showed a
decreased respiration rate. The latter was taken to support
the tacit assumption that NDH-1 was the major respiratory electron transport route into the PQ pool in
cyanobacteria as it is in many other bacteria and in
mitochondria from most eukaryotes. However, this view
was challenged when mutants lacking succinate dehydrogenase activity showed a very slow rate of respiratory
electron ow into the PQ pool (Cooley et al., 2000). As will
be argued in a subsequent section, this suggests that NDH1 activity in cyanobacteria in vivo is only very modest, and
that most respiratory electrons enter the PQ pool via SDH.
In cyanobacteria, NADPH is not used as a preferential
respiratory substrate but rather is applied for the CO2
xation process. However, a large number (46) of
isogenes for two of the NDH-1 subunits are present in
the Synechocystis genome; these isogenes may have
dierent functions (Ohkawa et al., 2000). This suggests
that NDH-1 may function in dierent capacities depending
on the physiological state of the cell.
According to the genomic sequence of Synechocystis sp.
PCC 6803, this cyanobacterium is capable of producing
type-2 NDH (NDH-2), which is a single-subunit protein
and that may not contribute to a proton gradient over the
thylakoid membrane. Three genes for NDH-2s are present
in the Synechocystis sp. PCC 6803 genome, but so far no
evidence has been found that would suggest a large activity

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Photosynthesis and Respiration in Cyanobacteria

of NDH-2 in providing electrons to the PQ pool. Instead,

NDH-2 in cyanobacteria may have a mostly regulatory
function (Howitt et al., 1999).

Succinate dehydrogenase
Genes for soluble SDH subunits are easily identied in the
Synechocystis sp. PCC 6803 genome, and upon deletion of
such genes a phenotype consistent with a lack of SDH
activity is found. Whereas fumarate (the SDH product) is
depleted in mutants lacking SDH, succinate accumulates
(Cooley et al., 2000). Moreover, in such mutants succinate
accumulates to a higher degree when 2-oxoglutarate (an
intermediate in the citric acid cycle before succinate) is
added, signifying the capability of cyanobacteria to
convert 2-oxoglutarate to succinate (Cooley et al., 2000)
even though a traditional 2-oxoglutarate dehydrogenase is
absent according to the genome sequence. This implies that
cyanobacteria can utilize a modied citric acid cycle and
that succinate and SDH are potentially important in
cyanobacterial respiratory metabolism.
In the Synechocystis mutant lacking SDH activity, the
rate of initial respiratory electron ow into the PQ pool was
about an order of magnitude lower than in wild type,
suggesting that essentially all respiratory electrons enter
the PQ pool through SDH activity rather than through
oxidation of NAD(P)H (Cooley et al., 2000). Therefore,
the large eect of inactivation of ndhB (an NDH-1 gene; see
above) on respiration may be an indirect eect due to the
absence of succinate in this mutant: oxidized NAD(P) is
needed for running the citric acid cycle and other
respiratory processes. This highlights the complexity of
metabolism even in rather simple organisms, and cautions
against one-sided interpretations. However, the biochemical analysis of Synechocystis mutants specically lacking
particular subunits provides an opportunity to critically
test previous and current hypotheses and interpretations.

Terminal oxidases
Using molecular-genetic approaches and the analysis of
specic mutants, the nature and relative activity of
terminal oxidases in Synechocystis sp. PCC 6803 has been
claried. According to biochemical data preceding the
availability of the genomic sequence of this organism, a
cytochrome aa3-type cytochrome-c oxidase was found to
be present along with another terminal oxidase (see
Schmetterer (1994) for a review). According to the genome
sequence, apart from a cytochrome-c oxidase there may be
a cytochrome bd-type quinol oxidase as well as a second
quinol oxidase that most resembles a cytochrome bo-type
oxidase. The cytochrome bd-type quinol oxidase could be
demonstrated on the basis of inhibitor studies as well as by
mutant analysis, but the cytochrome bo-type oxidase does
not appear to be expressed under the conditions used thus
4

far. Interestingly, under the conditions used, the cytochrome bd-type quinol oxidase appears to be located
predominantly in the cytoplasmic membrane, whereas
signicant cytochrome oxidase activity is seen in thylakoids (Howitt and Vermaas, 1998). Indeed, in mutants
lacking PS I, rapid (40 ms) electron ow from PS II to
cytochrome oxidase can be demonstrated, indicating a
close functional relationship between PS II and thylakoidlocalized cytochrome oxidase (Vermaas et al., 1994).
The presence of cytochrome oxidase in the cyanobacterial thylakoid membrane raises the question of what the
electron donor may be. If cytochrome c553, the luminal
electron carrier that can replace plastocyanin, is present,
then this is the likely electron donor. However, electron
transfer to the oxidase can also occur in the absence of this
cytochrome. This electron transfer appears to involve
plastocyanin, but also seems to require another cytochrome, cytochrome cM. This cytochrome c may serve as
an electron transport intermediate and might be associated
with the cytochrome oxidase complex (Manna and
Vermaas, 1997). Limited sequence similarity exists between cytochrome cM and the cytochrome c-binding part
of the cytochrome caa3-containing cytochrome-c oxidase
from bacteria with such a complex, and cytochrome cM
appears to be required for electron ow out of the PQ pool
under conditions that PS I and cytochrome c553 are absent
(Manna and Vermaas, 1997).

Components Involved in Both

Photosynthesis and Respiration
The plastoquinone pool
In Synechocystis sp. PCC 6803, apart from PQ the only
quinone found in thylakoids is vitamin K1 associated with
PS I. Therefore, essentially all electron transport through
unbound quinones appears to proceed via PQ in cyanobacterial thylakoids. Plastoquinone in the thylakoid
membrane shuttles electrons from both photosynthetic
and respiratory electron transport chains to the cytochrome b6f complex. PQ is reduced to the quinol form by
accepting two reducing equivalents, but, when bound to
protein, the semiquinone form (the radical form with one
electron more than the quinone and one electron less than
the quinol) can be stabilized. Therefore, PQ can function as
an adapter converting one-electron redox reactions (as
they occur, for example, in PS II and cytochrome b6f) to
two-electron reactions and vice versa.

The cytochrome b6f complex

A key complex in both photosynthetic and respiratory
electron transfer in cyanobacteria is the cytochrome b6f
complex. Eorts to fully inactivate this complex in
cyanobacteria have been unsuccessful thus far, indicating

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Photosynthesis and Respiration in Cyanobacteria

the central role this complex plays in electron transport.

Indeed, all electron transfer in photosynthesis and
respiration, with the exception of respiratory electron
ow to quinol oxidases, needs to proceed through the
cytochrome b6f complex. However, as quinol oxidase
may not be prevalent in thylakoids under many growth
conditions and may occur predominantly in cytoplasmic
membranes (Howitt and Vermaas, 1998), essentially all
plastoquinol oxidation in thylakoids occurs via the
cytochrome b6f complex in wild type under most growth
conditions.
The redox-active components of the cytochrome b6f
complex are associated with the cytochrome b6 apoprotein,
the cytochrome f apoprotein, and the Rieske FeS centre.
A fourth major component, subunit IV, does not carry
redox-active cofactors. In mitochondria and Gramnegative bacteria containing a bc1 complex, cytochrome
b6 and subunit IV are fused. Another interesting feature
when comparing cytochrome b6f and cytochrome bc1
complexes is that cytochrome f and cytochrome c1 do not
have a common ancestor, in spite of their homologous
function. In line with the dierent origins of the two
cytochromes, in cytochrome f the N-terminal amino
group of the processed protein forms a covalent bond
with the haem group, whereas this is not the case for
cytochrome c1.
Perhaps the cyanobacterial mutant generated thus far
with the lowest amount of cytochrome b6f activity is one
where ccsB, a gene coding for a protein involved in
maturation of cytochrome f, has been impaired (Tichy and
Vermaas, 1999). This mutant contains an N-terminally
modied CcsB that stabilizes preapocytochrome f but that
is inecient in maturation of the cytochrome (N-terminal
processing and covalent attachment of the haem). Consequently, the ccsB mutant accumulates preapocytochrome
f and has about a 5-fold reduced amount of mature,
functional cytochrome b6f. This strain grows only
microaerobically, and partial restoration of CcsB function
also restores the ability to grow aerobically. The role
of oxygen remains to be elucidated, but it may involve
regulation of gene expression.
An interesting feature of the cyanobacterial cytochrome b6f complex is that in the Synechocystis sp. PCC
6803 genome three genes are found that may code for
Rieske FeS centres, whereas only a single set of genes is
present for the other components of the complex. One
possible reason for this unexpected complexity is that
the dierent Rieske FeS centres dier in their interaction of the cytochrome b6f complex with soluble carriers,
thus providing a mechanism for regulation of electron
ow to PS I versus to the terminal cytochrome oxidase.

Soluble electron carriers

Both plastocyanin and cytochrome c553 can function in
both photosynthesis and respiratory electron transport.
In mutants lacking PS I, the gene for either soluble redox
carrier can be deleted with only a moderate eect on the
rate of electron ow from PS II via the quinone pool,
the cytochrome b6f complex and the remaining soluble
carrier to the cytochrome aa3-type cytochrome oxidase.
In mutants lacking either plastocyanin or cytochrome c553,
photosynthetic electron transport rates remain normal,
indicating that either of the two soluble carriers is
sucient.
Interestingly, eorts to delete the genes for both
plastocyanin and cytochrome c553 in the same strain have
been unsuccessful, indicating that one of the two carriers
is required to shuttle electrons to PS I and cytochrome
oxidase.

Regulation of Photosynthesis and

Respiration
A central question that will now need to be addressed is
how photosynthesis and respiration are regulated in a
cyanobacterium. For regulation, an important issue is the
capacity and rate of the various steps. The approximate
capacities of electron transfer steps in Synechocystis sp.
PCC 6803 are summarized in Table 2. The actual rate of the
reactions may be signicantly lower in vivo, depending on
the conditions (light intensity, redox state, etc.). From
Table 2, it is clear that PS I activity is abundant relative to
that of the cytochrome b6f complex, and this may explain in
part the slow P700 1 rereduction kinetics (100200 ms
half-time) that are generally observed after a period of
illumination. If light is abundant, the photosynthetic
electron transport chain has a much higher capacity of
electron ow than has the respiratory chain, but at very low
light intensity or in darkness respiratory rates are higher
than those of photosynthesis. As the capacities of
cytochrome oxidase and succinate dehydrogenase seem
comparable, respiratory electron ow will not lead to
major changes in the redox state of the PQ pool (overreduction or overoxidation), leaving room for regulation
of metabolic processes that are apparently mediated via the
PQ redox state.

Parallels to the Situation in Chloroplasts

An important question is that of the relevance of the
insights obtained thus far on Synechocystis for electron
transport events in other organisms, such as plants. In
photosynthetic eukaryotes, photosynthetic and respiratory electron ows have been separated as they occur in
two dierent organelles. However, chloroplasts retain

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Photosynthesis and Respiration in Cyanobacteria

Table 2 Approximate capacity and probable source of rate limitation of photosynthetic and
respiratory electron transfer in Synechocystis sp. PCC 6803. (For simplicity, these values have been
expressed on a per-chlorophyll basis)
Complex

Capacity (mol electrons

h1 per mg chlorophyll)

Photosystem II

1000

Succinate dehydrogenase

200

NADPH dehydrogenase

20

Cytochrome b6 f complex
Photosystem I
Cytochrome-c oxidase

1000
3000
200

certain cyanobacterial features involved in respiratory

electron ow. For example, genes for the NDH-1 complex
are retained in the chloroplast genome, and a small amount
of NDH-1 activity can be demonstrated (Burrows et al.,
1998). However, there is little evidence for signicant
activity of SDH or of a terminal oxidase in chloroplasts
under normal conditions. None the less, the case for
respiratory activity in chloroplasts (chlororespiration) is
slowly building, even though it may not involve the same
components that are prevalent in cyanobacteria (for
example, Cournac et al., 2000). However, it is likely that
comparisons with the cyanobacterial system will further
guide the search for components involved in such activities
in chloroplasts.

Acknowledgements
The work from my group referred to here has been funded
mostly by grants from the US Department of Agriculture
Competitive Research Grants Program (9701526) and the
Human Frontiers Science Program Organization (RG
0051/97). A research fellowship from the Alexander-vonHumboldtstiftung is gratefully acknowledged.

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Further Reading
Bryant DA (1994) The Molecular Biology of Cyanobacteria. Dordrecht:
Kluwer Academic Publishers.
Madigan MT, Martinko JM and Parker J (1997) Brock Biology of
Microorganisms, 8th edn. Upper Saddle River, New Jersey: Prentice
Hall.
Ort DR and Yocum CF (1996) Oxygenic Photosynthesis: The Light
Reactions. Dordrecht: Kluwer Academic Publishers.
White D (2000) The Physiology and Biochemistry of Prokaryotes, 2nd
edn. New York: Oxford University Press.

ENCYCLOPEDIA OF LIFE SCIENCES / & 2001 Macmillan Publishers Ltd, Nature Publishing Group / www.els.net